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Literature summary for 3.4.14.9 extracted from

  • Guhaniyogi, J.; Sohar, I.; Das, K.; Stock, A.M.; Lobel, P.
    Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis (2009), J. Biol. Chem., 284, 3985-3997.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.14.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in CHO cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
deglycosylated inactive proenzyme pro-TPP1, hanging drop vapour diffusion method, using 0.1 M citrate, 4-7% polyethylene glycol 6000, at pH 5.0 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O14773
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
butyl-Sepharose 4 column chromatography, Mono Q12 column chromatography, and Superdex 75 gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
 ?
L-Arg-L-Nle-L-Nle-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens L-Arg-L-Nle-L-Nle + 7-amino-4-methylcoumarin
-
 ?

Synonyms

Synonyms Comment Organism
Tpp1 TPP1 is a serine protease that possesses two catalytic functions, a primary tripeptidyl exopeptidase activity with a pH optimum of about 5.0 that catalyzes the sequential release of tripeptides from the unsubstituted N termini of substrates and a much weaker endoproteolytic activity with a pH optimum of about 3.0 Homo sapiens
tripeptidyl-peptidase 1
-
 Homo sapiens